Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.
Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.
复制标题
野生酵母具有多种独特的淀粉样蛋白结构,具有很强的朊病毒诱导能力。
DOI:
10.1111/mmi.12543
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发表时间:
2014
影响因子:
3.6
通讯作者:
True,HeatherL
中科院分区:
文献类型:
--
作者:
Westergard,Laura;True,HeatherL
Variation in amyloid structures profoundly influences a wide array of pathological phenotypes in mammalian protein conformation disorders and dominantly inherited phenotypes in yeast. Here, we describe, for the first time, naturally occurring, self‐propagating, structural variants of a prion protein isolated from wild strains of the yeastSaccharomyces cerevisiae. Variants of the [RNQ+] prion propagating in a variety of wild yeast differ biochemically, in their intracellular distributions, and in their ability to promote formation of the [PSI+] prion. [PSI+] is an epigenetic regulator of cellular phenotype and adaptability. Strikingly, we find that most natural [RNQ+] variants induced [PSI+] at high frequencies and the majority of [PSI+] variants elicited strong cellular phenotypes. We hypothesize that the presence of an efficient [RNQ+] template primes the cell for [PSI+] formation in order to induce [PSI+] in conditions where it would be advantageous. These studies utilize naturally occurring structural variants to expand our understanding of the consequences of diverse prion conformations on cellular phenotypes.